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Conserved domains on  [gi|568967951|ref|XP_006513896|]
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core histone macro-H2A.2 isoform X1 [Mus musculus]

Protein Classification

HFD_H2A and Macro_SF domain-containing protein( domain architecture ID 10049445)

HFD_H2A and Macro_SF domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Macro_SF super family cl00019
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 178-326 1.46e-84

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


The actual alignment was detected with superfamily member cd02904:

Pssm-ID: 469581  Cd Length: 188  Bit Score: 253.00  E-value: 1.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 178 GPGDGFTILSSKSLVLGQKLSLTQSDIshiGSMRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKSQGPLEV 257
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQKLTVVQGDI---ASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEV 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967951 258 AEAAVSQSSGLAAKFVIHCHIPQWGSDKCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSGSKLLPTHPA 326
Cdd:cd02904   78 AGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTA 146
H2A smart00414
Histone 2A;
14-119 1.39e-59

Histone 2A;


:

Pssm-ID: 197711  Cd Length: 106  Bit Score: 186.39  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951    14 SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 568967951    94 LLKGVTIASGGVLPRIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
 
Name Accession Description Interval E-value
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 178-326 1.46e-84

macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant.


Pssm-ID: 394875  Cd Length: 188  Bit Score: 253.00  E-value: 1.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 178 GPGDGFTILSSKSLVLGQKLSLTQSDIshiGSMRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKSQGPLEV 257
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQKLTVVQGDI---ASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEV 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967951 258 AEAAVSQSSGLAAKFVIHCHIPQWGSDKCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSGSKLLPTHPA 326
Cdd:cd02904   78 AGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTA 146
H2A smart00414
Histone 2A;
14-119 1.39e-59

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 186.39  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951    14 SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 568967951    94 LLKGVTIASGGVLPRIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PTZ00017 PTZ00017
histone H2A; Provisional
 2-125 3.00e-56

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 179.17  E-value: 3.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   2 SGRSGKKKMSK---LSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAP 78
Cdd:PTZ00017   4 KGKTGGGKAGKkkpVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568967951  79 RHILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSE 125
Cdd:PTZ00017  84 RHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKK 130
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 14-101 1.80e-48

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467020  Cd Length: 89  Bit Score: 157.31  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951  14 SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQ 93
Cdd:cd00074    2 SRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELNK 81


                 ....*...
gi 568967951  94 LLKGVTIA 101
Cdd:cd00074   82 LFKGVTIA 89
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-128 8.10e-46

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 152.32  E-value: 8.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   3 GRSGKKKMSKL--SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRH 80
Cdd:COG5262    5 GKGGKAADARVsqSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRH 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568967951  81 ILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSETIL 128
Cdd:COG5262   85 LQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 216-326 7.90e-27

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 101.87  E-value: 7.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951  216 VHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKsqGPLEVAEAAVSQSSGLAAKFVIHCHIPQW---GSDKCEEQLEE 292
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWrhgGSHGEEELLES 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568967951  293 TIKNCLSAAEDKKLKSVAFPPFPSGSKLLPTHPA 326
Cdd:pfam01661  79 CYRNALALAEELGIKSIAFPAISTGIYGFPWEEA 112
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 196-317 3.33e-17

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 76.58  E-value: 3.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   196 KLSLTQSDISHIgsmRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLEtvKELRKS-QGPLEVAEAAVSQSSGLAAKFVI 274
Cdd:smart00506   1 ILKVVKGDITKP---RADAIVNAANSDGAHGGGVAGAIARAAGKALSK--EEVRKLaGGECPVGTAVVTEGGNLPAKYVI 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 568967951   275 HCHIPQWGSD--KCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSG 317
Cdd:smart00506  76 HAVGPRASGHskEGFELLENAYRNCLELAIELGITSVALPLIGTG 120
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 197-313 3.78e-16

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 74.83  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 197 LSLTQSDIShigSMRVEGIVHPTTAE------IDLkeeigkALEKAGGKEFLETVKELRKsQGPLEVAEAAVSQSSGLAA 270
Cdd:COG2110    1 IEIVQGDIT---ELDVDAIVNAANSSllggggVAG------AIHRAAGPELLEECRRLCK-QGGCPTGEAVITPAGNLPA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568967951 271 KFVIHCHIPQW--GSDKCEEQLEETIKNCLSAAEDKKLKSVAFPP 313
Cdd:COG2110   71 KYVIHTVGPVWrgGGPSEEELLASCYRNSLELAEELGIRSIAFPA 115
PRK00431 PRK00431
ADP-ribose-binding protein;
232-312 8.76e-16

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 74.11  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 232 ALEKAGGKEFLETVKELRKSQGPLEVAEAAVSQSSGLAAKFVIHCHIPQW--GSDKCEEQLEETIKNCLSAAEDKKLKSV 309
Cdd:PRK00431  37 AIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTVGPVWrgGEDNEAELLASAYRNSLRLAAELGLRSI 116


                 ...
gi 568967951 310 AFP 312
Cdd:PRK00431 117 AFP 119
Histone_H2A_C pfam16211
C-terminus of histone H2A;
89-123 3.39e-14

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 65.63  E-value: 3.39e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568967951   89 EELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGK 123
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
 
Name Accession Description Interval E-value
Macro_H2A-like cd02904
macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with ...
 178-326 1.46e-84

macrodomain, macroH2A-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family are similar to macroH2A, a variant of the major-type core histone H2A, which contains an N-terminal H2A domain and a C-terminal nonhistone macrodomain. Histone macroH2A is enriched on the inactive X chromosome of mammalian female cells. It does not bind poly ADP-ribose, but does bind the monomeric SirT1 metabolite O-acetyl-ADP-ribose (OAADPR) with high affinity through its macrodomain. This family also includes the ADP-ribose binding macrodomain of the macroH2A variant, macroH2A1.1. The macroH2A1.1 isoform inhibits PARP1-dependent DNA-damage induced chromatin dynamics. The putative ADP-ribose binding pocket of the human macroH2A2 macrodomain exhibits marked structural differences compared with the macroH2A1.1 variant.


Pssm-ID: 394875  Cd Length: 188  Bit Score: 253.00  E-value: 1.46e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 178 GPGDGFTILSSKSLVLGQKLSLTQSDIshiGSMRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKSQGPLEV 257
Cdd:cd02904    1 GPGDGFTILSEKKLFLGQKLTVVQGDI---ASIKADAIVHPTNATFYLGGEVGSALEKAGGKEFVEEVKELRKSNGPLEV 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568967951 258 AEAAVSQSSGLAAKFVIHCHIPQWGSDKCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSGSKLLPTHPA 326
Cdd:cd02904   78 AGAAISPGHNLPAKFVIHCNSPSWGSDKCEELLEKTVKNCLALADEKKLKSVAFPSIGSGRNGFPKQTA 146
H2A smart00414
Histone 2A;
14-119 1.39e-59

Histone 2A;


Pssm-ID: 197711  Cd Length: 106  Bit Score: 186.39  E-value: 1.39e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951    14 SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQ 93
Cdd:smart00414   1 SRSARAGLQFPVGRIHRLLRKGTYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKRRITPRHLQLAIRNDEELNK 80

                           90       100
                   ....*....|....*....|....*.
gi 568967951    94 LLKGVTIASGGVLPRIHPELLAKKRG 119
Cdd:smart00414  81 LLKGVTIAQGGVLPNIHKVLLPKKTG 106
PTZ00017 PTZ00017
histone H2A; Provisional
 2-125 3.00e-56

histone H2A; Provisional


Pssm-ID: 185399  Cd Length: 134  Bit Score: 179.17  E-value: 3.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   2 SGRSGKKKMSK---LSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAP 78
Cdd:PTZ00017   4 KGKTGGGKAGKkkpVSRSAKAGLQFPVGRVHRYLKKGRYAKRVGAGAPVYLAAVLEYLTAEVLELAGNAAKDNKKKRITP 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568967951  79 RHILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSE 125
Cdd:PTZ00017  84 RHIQLAIRNDEELNKLLAGVTIASGGVLPNIHKVLLPKKSKPKQGKK 130
PLN00157 PLN00157
histone H2A; Provisional
 1-126 1.28e-54

histone H2A; Provisional


Pssm-ID: 177758  Cd Length: 132  Bit Score: 174.65  E-value: 1.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   1 MSGR----SGKKKMSKLSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARI 76
Cdd:PLN00157   1 MSGRgkrkGGGGGKKATSRSAKAGLQFPVGRIARYLKAGKYATRVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKSRI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568967951  77 APRHILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSET 126
Cdd:PLN00157  81 VPRHIQLAVRNDEELSKLLGGVTIAAGGVLPNIHSVLLPKKSGKSKGEPK 130
HFD_H2A cd00074
histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core ...
 14-101 1.80e-48

histone-fold domain found in histone H2A and similar proteins; Histone H2A is the core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467020  Cd Length: 89  Bit Score: 157.31  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951  14 SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQ 93
Cdd:cd00074    2 SRSKRAGLQFPVGRIHRLLKKGTYAKRVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKKRITPRHIQLAIRNDEELNK 81


                 ....*...
gi 568967951  94 LLKGVTIA 101
Cdd:cd00074   82 LFKGVTIA 89
PLN00156 PLN00156
histone H2AX; Provisional
 3-125 2.34e-48

histone H2AX; Provisional


Pssm-ID: 215080  Cd Length: 139  Bit Score: 158.98  E-value: 2.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   3 GRSGKKKMSK-LSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHI 81
Cdd:PLN00156   9 GGRGKPKATKsVSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLSAVLEYLAAEVLELAGNAARDNKKNRIVPRHI 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568967951  82 LLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGtKGKSE 125
Cdd:PLN00156  89 QLAVRNDEELSKLLGSVTIAAGGVLPNIHQTLLPKKVG-KGKGD 131
HTA1 COG5262
Histone H2A [Chromatin structure and dynamics];
3-128 8.10e-46

Histone H2A [Chromatin structure and dynamics];


Pssm-ID: 227587 [Multi-domain]  Cd Length: 132  Bit Score: 152.32  E-value: 8.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   3 GRSGKKKMSKL--SRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRH 80
Cdd:COG5262    5 GKGGKAADARVsqSRSAKAGLIFPVGRVKRLLKKGNYRMRIGAGAPVYLAAVLEYLAAEILELAGNAARDNKKKRIIPRH 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568967951  81 ILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSETIL 128
Cdd:COG5262   85 LQLAIRNDEELNKLLGDVTIAQGGVLPNINPGLLPKSSKKGSKRSQEL 132
PLN00153 PLN00153
histone H2A; Provisional
 1-125 1.59e-43

histone H2A; Provisional


Pssm-ID: 165721 [Multi-domain]  Cd Length: 129  Bit Score: 146.02  E-value: 1.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   1 MSGRSGKKKMSK--LSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAP 78
Cdd:PLN00153   1 MAGRGKGKTSGKkaVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYLTAEVLELAGNAARDNKKNRIVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568967951  79 RHILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKK-RGTKGKSE 125
Cdd:PLN00153  81 RHIQLAIRNDEELGKLLGEVTIASGGVLPNIHAVLLPKKtKGGKGEET 128
PLN00154 PLN00154
histone H2A; Provisional
 2-116 4.11e-31

histone H2A; Provisional


Pssm-ID: 177756  Cd Length: 136  Bit Score: 114.27  E-value: 4.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   2 SGRSGKKKMSK---LSRSARAGVIFPVGRLMRYLKKGTFKY-RISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIA 77
Cdd:PLN00154  15 TAAAAKKDKDKkkpTSRSSRAGLQFPVGRIHRQLKQRVSAHgRVGATAAVYTAAILEYLTAEVLELAGNASKDLKVKRIT 94

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568967951  78 PRHILLAVANDEELNQLLKGvTIASGGVLPRIHPELLAK 116
Cdd:PLN00154  95 PRHLQLAIRGDEELDTLIKG-TIAGGGVIPHIHKSLINK 132
PTZ00252 PTZ00252
histone H2A; Provisional
 4-126 7.36e-29

histone H2A; Provisional


Pssm-ID: 240330  Cd Length: 134  Bit Score: 108.13  E-value: 7.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   4 RSGKKKMSK--LSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDN--KKARIAPR 79
Cdd:PTZ00252   5 KQAKKKASKsgSGRSAKAGLIFPVGRVGSLLRRGQYARRIGASGAVYMAAVLEYLTAELLELSVKAAAQQakKPKRLTPR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568967951  80 HILLAVANDEELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGKSET 126
Cdd:PTZ00252  85 TVTLAVRHDDDLGSLLKNVTLSRGGVMPSLNKALAKKHKSGKKAKAT 131
Macro pfam01661
Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ...
 216-326 7.90e-27

Macro domain; The Macro or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose (an NAD metabolite) or related ligands. Binding to ADP-ribose could be either covalent or non-covalent: in certain cases it is believed to bind non-covalently; while in other cases (such as Aprataxin) it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein. This domain is found in a number of otherwise unrelated proteins. It is found at the C-terminus of the macro-H2A histone protein 4 and also in the non-structural proteins of several types of ssRNA viruses such as NSP3 from alpha-viruses and coronaviruses. This domain is also found on its own in a family of proteins from bacteria, archaebacteria and eukaryotes. The 3D structure of the SARS-CoV Macro domain has a mixed alpha/beta fold consisting of a central seven-stranded twisted mixed beta sheet sandwiched between two alpha helices on one face, and three on the other. The final alpha-helix, located on the edge of the central beta-sheet, forms the C terminus of the protein. The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. Several Macro domain only proteins are shorter than AF1521, and appear to lack either the first strand of the beta-sheet or the C-terminal helix 5. Well conserved residues form a hydrophobic cleft and cluster around the AF1521-ADP-ribose binding site.


Pssm-ID: 460286  Cd Length: 116  Bit Score: 101.87  E-value: 7.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951  216 VHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKsqGPLEVAEAAVSQSSGLAAKFVIHCHIPQW---GSDKCEEQLEE 292
Cdd:pfam01661   1 VNAANSRLLGGGGVAGAIHRAAGPELLEECRELKK--GGCPTGEAVVTPGGNLPAKYVIHTVGPTWrhgGSHGEEELLES 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568967951  293 TIKNCLSAAEDKKLKSVAFPPFPSGSKLLPTHPA 326
Cdd:pfam01661  79 CYRNALALAEELGIKSIAFPAISTGIYGFPWEEA 112
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 215-317 1.18e-21

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 88.61  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 215 IVHPTTAEIDLKEEIGKALEKAGGKEFLETVkELRKSQGPLEVAEAAVSQSSGLAAKFVIHCHIPQWGSDK-CEEQLEET 293
Cdd:cd02749    3 IVNPANNDLYLGGGVAKAISKKAGGDLQEEC-EERKKNGYLKVGEVAVTKGGNLPARYIIHVVGPVASSKKkTYEPLKKC 81

                         90       100
                 ....*....|....*....|....
gi 568967951 294 IKNCLSAAEDKKLKSVAFPPFPSG 317
Cdd:cd02749   82 VKNCLSLADEKGLKSVAFPAIGTG 105
Macro_Af1521_BAL-like cd02907
macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse ...
 194-317 1.86e-19

macrodomain, Af1521-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. The macrodomains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macrodomain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward ADP-ribose-1"-monophosphate (Appr-1"-p). Also included in this family are the N-terminal (or first) macrodomains of BAL (B-aggressive lymphoma) proteins which contain multiple macrodomains, such as the first macrodomain of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394877 [Multi-domain]  Cd Length: 158  Bit Score: 83.69  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 194 GQKLSLTQSDISHigsMRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKSQGPLEVAEAAVSQSSGLAAKFV 273
Cdd:cd02907    1 GIKVSVYKGDITK---EKVDAIVNAANERLKHGGGVAGAISKAGGPEIQEECDKYIKKNGKLRVGEVVVTSAGKLPCKYV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568967951 274 IHCHIPQWGSDK---CEEQLEETIKNCLSAAEDKKLKSVAFPPFPSG 317
Cdd:cd02907   78 IHAVGPRWSGGSkeeCEDLLYKAVLNSLEEAEELKATSIAIPAISSG 124
A1pp smart00506
Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by ...
 196-317 3.33e-17

Appr-1"-p processing enzyme; Function determined by Martzen et al. Extended family detected by reciprocal PSI-BLAST searches (unpublished results, and Pehrson _ Fuji).


Pssm-ID: 214701  Cd Length: 133  Bit Score: 76.58  E-value: 3.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951   196 KLSLTQSDISHIgsmRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLEtvKELRKS-QGPLEVAEAAVSQSSGLAAKFVI 274
Cdd:smart00506   1 ILKVVKGDITKP---RADAIVNAANSDGAHGGGVAGAIARAAGKALSK--EEVRKLaGGECPVGTAVVTEGGNLPAKYVI 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 568967951   275 HCHIPQWGSD--KCEEQLEETIKNCLSAAEDKKLKSVAFPPFPSG 317
Cdd:smart00506  76 HAVGPRASGHskEGFELLENAYRNCLELAIELGITSVALPLIGTG 120
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 197-313 3.78e-16

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 74.83  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 197 LSLTQSDIShigSMRVEGIVHPTTAE------IDLkeeigkALEKAGGKEFLETVKELRKsQGPLEVAEAAVSQSSGLAA 270
Cdd:COG2110    1 IEIVQGDIT---ELDVDAIVNAANSSllggggVAG------AIHRAAGPELLEECRRLCK-QGGCPTGEAVITPAGNLPA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568967951 271 KFVIHCHIPQW--GSDKCEEQLEETIKNCLSAAEDKKLKSVAFPP 313
Cdd:COG2110   71 KYVIHTVGPVWrgGGPSEEELLASCYRNSLELAEELGIRSIAFPA 115
PRK00431 PRK00431
ADP-ribose-binding protein;
232-312 8.76e-16

ADP-ribose-binding protein;


Pssm-ID: 234759  Cd Length: 177  Bit Score: 74.11  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 232 ALEKAGGKEFLETVKELRKSQGPLEVAEAAVSQSSGLAAKFVIHCHIPQW--GSDKCEEQLEETIKNCLSAAEDKKLKSV 309
Cdd:PRK00431  37 AIHRAAGPEILEECRELRQQQGPCPTGEAVITSAGRLPAKYVIHTVGPVWrgGEDNEAELLASAYRNSLRLAAELGLRSI 116


                 ...
gi 568967951 310 AFP 312
Cdd:PRK00431 117 AFP 119
PLN00155 PLN00155
histone H2A; Provisional
 1-56 8.76e-15

histone H2A; Provisional


Pssm-ID: 165723  Cd Length: 58  Bit Score: 67.81  E-value: 8.76e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568967951   1 MSGRSGKKKMSK--LSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYL 56
Cdd:PLN00155   1 MAGRGKGKTSGKkaVSRSAKAGLQFPVGRIARYLKKGKYAERIGAGAPVYLAAVLEYL 58
HFD_SOS1_rpt2 cd22915
second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; ...
 22-95 1.73e-14

second histone-fold domain found in son of sevenless homolog 1 (SOS-1) and similar proteins; SOS-1 is a guanine nucleotide exchange factor for Ras that binds to GRB2. It promotes the exchange of Ras-bound GDP by GTP. It is a catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac, by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity. SOS-1 contains tandem histone folds at the N-terminal region. The model corresponds to the second repeat.


Pssm-ID: 467040  Cd Length: 75  Bit Score: 67.65  E-value: 1.73e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568967951  22 IFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQLL 95
Cdd:cd22915    1 LFPVDKIHPLLKKDLLVYKVDPQVSLYLVAVLEYIAADILKLAGNYVRNIRHYEITSQDIKVAMCADKVLMDLF 74
Histone_H2A_C pfam16211
C-terminus of histone H2A;
89-123 3.39e-14

C-terminus of histone H2A;


Pssm-ID: 465070  Cd Length: 35  Bit Score: 65.63  E-value: 3.39e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568967951   89 EELNQLLKGVTIASGGVLPRIHPELLAKKRGTKGK 123
Cdd:pfam16211   1 EELNKLLRGVTIAQGGVLPNIHKVLLPKKTKKKKK 35
Macro_OAADPr_deacetylase cd02908
macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of ...
 196-312 6.89e-12

macrodomain, O-acetyl-ADP-ribose (OAADPr) family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacetylases may reverse cellular ADP-ribosylation.


Pssm-ID: 438955  Cd Length: 166  Bit Score: 62.92  E-value: 6.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 196 KLSLTQSDISHigsMRVEGIVHPttAE--------IDlkeeigKALEKAGGKEFLETVKELRksqGPLEVAEAAVSQSSG 267
Cdd:cd02908    1 KISLWRGDITK---LEVDAIVNA--ANssllggggVD------GAIHRAAGPELLEECRKLG---GVCPTGEAKITPGYN 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568967951 268 LAAKFVIHCHIPQW--GSDKCEEQLEETIKNCLSAAEDKKLKSVAFP 312
Cdd:cd02908   67 LPAKYVIHTVGPIGegGVEEEPELLASCYRSSLELALENGLKSIAFP 113
Histone pfam00125
Core histone H2A/H2B/H3/H4;
7-85 2.93e-11

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 60.14  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951    7 KKKMSKLSRSARAGVIFPVGRLMRYLKKGTFK-YRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAV 85
Cdd:pfam00125  44 KEIRKYQSSTDLLIYKLPFARVVREVVQSTKTdLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLAR 123
Macro_BAL-like cd02903
macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of ...
 196-322 1.89e-09

macrodomain, B-aggressive lymphoma (BAL)-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to BAL (B-aggressive lymphoma) proteins, which contain one to three macrodomains. Most BAL family macrodomains belong to this family except for the most N-terminal domain in multiple-domain containing proteins. This family includes the second and third macrodomains of mono-ADP-ribosyltransferase PARP14 (PARP-14, also known as ADP-ribosyltransferase diphtheria toxin-like 8, ATRD8, B aggressive lymphoma protein 2, or BAL2). Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcriptional repressors.


Pssm-ID: 394874  Cd Length: 175  Bit Score: 56.11  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 196 KLSLTQSDISHIgsmRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLETVKELRKSQGPLEVAeaaVSQSSGLAAKFVIH 275
Cdd:cd02903    9 TVQLVKGDITKE---KTDVIVNSVSSDLLLKGGVSKAILKAAGPELQDECANQGKQPASGDVI---VTSGGNLPCKYVYH 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568967951 276 CHIPQWGSDKCEeQLEETIKNCLSAAEDKKLKSVAFPPFPSGSKLLP 322
Cdd:cd02903   83 VVLPHYNPGNEK-TLKDIVRKCLEKAENYKMSSISFPAIGTGNLGFP 128
HFD_ABTB2-like cd22913
histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) ...
 12-91 3.50e-09

histone-fold domain found in ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; ABTB2, also called Bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, which has implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). This subfamily also includes BTB/POZ domain-containing protein 11 (BTBD11), also called ankyrin repeat and BTB/POZ domain-containing protein BTBD11. It is a BTB-domain-containing Kelch-like protein with unknown function.


Pssm-ID: 467038  Cd Length: 105  Bit Score: 53.46  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951  12 KLSRSARAGVIFPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEEL 91
Cdd:cd22913    8 RRSKSARCGLTFSVGRFHRWMVDSRLAKRIHEHAAVYLTACMENLLEEIFLRALASLVPKGELELTVEALEYGINNDAEL 87
Macro_Ttha0132-like cd03330
Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein ...
 196-312 1.02e-08

Macrodomain, uncharacterized family similar to Thermus thermophilus hypothetical protein Ttha0132; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response. This family is composed of uncharacterized proteins containing a stand-alone macrodomain, similar to Thermus thermophilus hypothetical protein Ttha0132.


Pssm-ID: 394879  Cd Length: 147  Bit Score: 53.21  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 196 KLSLTQSDIShigSMRVEGIVHPTTAEIDLKEEIGKALEKAGGKE-FLETVKelrksQGPLEVAEAAVSQSSGLAAKFVI 274
Cdd:cd03330    1 RLIVVQGDIT---EQDADAIVNAANRRLLMGSGVAGAIKRKGGEEiEREAMR-----KGPIRVGEAVETGAGKLPAKYVI 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568967951 275 HCH-IPQWGSDKcEEQLEETIKNCLSAAEDKKLKSVAFP 312
Cdd:cd03330   73 HAAvMGMPGRSS-EESIRDATRNALAKAEELGLESVAFP 110
Macro_GDAP2-like cd02905
macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse ...
 195-326 1.42e-05

macrodomain, GDAP2-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family contains proteins similar to human GDAP2, the ganglioside induced differentiation associated protein 2, whose gene is expressed at a higher level in differentiated Neuro2a cells compared with non-differentiated cells. GDAP2 contains an N-terminal macrodomain and a C-terminal Sec14p-like lipid binding domain. It is specifically expressed in brain and testis.


Pssm-ID: 394876  Cd Length: 169  Bit Score: 44.53  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 195 QKLSLTQSDIShigSMRVEGIVHPTTAEIDLKEEIGKALEKAGGKEFLEtvkELRKsQGPLEVAEAAVSQSSGLAAKFVI 274
Cdd:cd02905    1 RKIVLWDGDLT---LLNVDAIVNSTNESLTDKSPISDRLFLAAGPELRE---ELAK-LGGCRTGEAKLTKGYNLPARYVI 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568967951 275 HCHIPQWgSDK----CEEQLEETIKNCLSAAEDKKLKSVAFPPFPSGSKLLPTHPA 326
Cdd:cd02905   74 HTVGPRY-NEKyrtaAESALYSCYRNVLQLAKEHKLRSVAFPVIHSERRGYPLEDG 128
PRK04143 PRK04143
protein-ADP-ribose hydrolase;
195-312 5.80e-05

protein-ADP-ribose hydrolase;


Pssm-ID: 235225  Cd Length: 264  Bit Score: 43.82  E-value: 5.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951 195 QKLSLTQSDISHigsMRVEGIV-----------HPTTAEIDlkeeigKALEKAGGKEFLETVKELRKSQGPLE-VAEAAV 262
Cdd:PRK04143  83 DNIFLWQGDITR---LKVDAIVnaansrllgcfQPNHDCID------NAIHTFAGVQLRLDCAEIMTEQGRKEaTGQAKI 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568967951 263 SQSSGLAAKFVIHCHIPQWG----SDKCEEQLEETIKNCLSAAEDKKLKSVAFP 312
Cdd:PRK04143 154 TRAYNLPAKYVIHTVGPIIRkqpvSPIRADLLASCYRSCLKLAEKAGLKSIAFC 207
BUR6 COG5247
Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];
23-108 9.25e-05

Class 2 transcription repressor NC2, alpha subunit (DRAP1 homolog) [Transcription];


Pssm-ID: 227572  Cd Length: 113  Bit Score: 41.10  E-value: 9.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568967951  23 FPVGRLMRYLKKGTFKYRISVGAPVYMAAVIEYLAAEILELAGNAARDNKKARIAPRHILLAVANDEELNQLLKGVTIAS 102
Cdd:COG5247   24 FPIARLKKIMQLDEDIGKVGQSTPVIASKALEMFLTEIVGLSLKEARKKSSKRMTSEFLKRATESDEKFDFLKNMEQFKN 103


                 ....*.
gi 568967951 103 GGVLPR 108
Cdd:COG5247  104 RETQPE 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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